Fluorescent methods to detect and discover peptide and protein interactions in vitro

Monday, 6 March – 4:00pm – 5:00pm HDR Seminar

Location: Chemistry Lecture Theatre 2 and Online (Zoom)

Speaker: Joy Ghrayche, University of Sydney

Host:  Prof. Elizabeth New

Abstract: Fluorescence spectroscopy has proven to be a powerful technique in the field of biology, providing a robust tool for investigating and understanding cellular function at the molecular level. Small molecule fluorophores in particular, have become a prominent tool in this field as they offer several advantages over traditional methods. Such methods usually require fixation or lysis to access cellular contents, making them unsuitable for visualising transient processes that are a pivotal feature of biological function.
Peptides and proteins are biomolecules that play a critical role in cellular function. They are responsible for a diverse range of biological functions including catalysis, structure, transport, signalling and defence. The unique properties of peptide and protein interactions have been exploited in the field of medicine for uses like protein-targeted therapeutics, and diagnostic agents. However, such developments would not be possible without an understanding of the specific functions of these biomolecules. Therefore, the study of proteins and their functions in the body is crucial for advancing our understanding of biological systems, and for developing new therapies and treatments for the betterment of human health.

In this work, novel fluorescent methods to study peptide and protein interactions were developed. Such methods included the: development of a multimodal fluorescent probe for mass spectrometry and fluorescence studies using a single sample; computational studies of novel fluorescent scaffolds for their utility as protein-specific redox sensors; development of a fluorescent label for facile identification of ligand-receptor interactions.